Trafficking Protein Particle Complex 2 (TRAPPC2), also known as Sedlin, is a crucial component of the trafficking protein particle (TRAPP) complex. This complex plays a significant role in the transport of proteins between cellular compartments, particularly between the endoplasmic reticulum (ER) and the Golgi apparatus .
TRAPPC2 is involved in the transport of large proteins, such as procollagens, from the ER to the Golgi apparatus. This transport is essential for the proper processing and modification of these proteins, which are later transformed into mature collagen. Collagen is vital for the strength and support of connective tissues, including skin, bone, cartilage, tendons, and ligaments .
Mutations in the TRAPPC2 gene can lead to X-linked spondyloepiphyseal dysplasia tarda, a condition that impairs bone growth and predominantly affects males. This condition usually manifests between the ages of 6 and 10 and is characterized by a lack of functional Sedlin protein, which disrupts the transport of procollagen and reduces the amount of mature collagen in cells .
The preparation of recombinant TRAPPC2 involves the expression of the protein in a suitable host, such as HEK293T cells. The recombinant protein is then purified using affinity chromatography techniques. The protein is typically stored at -80°C to maintain its stability and avoid repeated freeze-thaw cycles .
TRAPPC2 is part of the TRAPP complex, which regulates multiple membrane trafficking pathways. The TRAPP complexes exist in three forms, each activating specific GTPases such as Ypt1 or RAB1. These complexes play a crucial role in the secretory pathway, ensuring the directionality and fidelity of protein transport from the ER to the Golgi complex and beyond .